3.7.1.7: beta-diketone hydrolase
This is an abbreviated version!
For detailed information about beta-diketone hydrolase, go to the full flat file.
Word Map on EC 3.7.1.7
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3.7.1.7
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sphingopyxis
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textile
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putida
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lipase
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sludge
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shake
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cytochemically
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ache
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desizing
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acetylacetone
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gly-x-ser-x-gly
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p-nitrophenyl
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alpha-granules
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caprylate
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industry
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wastewater
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hydrolysed
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pmsf
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sphingomonas
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depolymerases
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dt
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molecular biology
- 3.7.1.7
- sphingopyxis
-
textile
- putida
- lipase
-
sludge
-
shake
-
cytochemically
-
ache
-
desizing
- acetylacetone
-
gly-x-ser-x-gly
- p-nitrophenyl
-
alpha-granules
- caprylate
- industry
-
wastewater
-
hydrolysed
- pmsf
- sphingomonas
-
depolymerases
- dt
- molecular biology
Reaction
Synonyms
ABDH, Alr4455 protein, beta-diketone hydrolase, OPH, OPH hydrolase, oxidized polyvinyl alcohol hydrolase, oxidized PVA hydrolase, oxidized-PVA hydrolase, poly(vinyl alcohol) (PVA)-degrading enzyme, pOPH, PVA-degrading enzyme, PVAase, sOPH
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General Information
General Information on EC 3.7.1.7 - beta-diketone hydrolase
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evolution
metabolism
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oxidized polyvinyl alcohol hydrolase is a key enzyme in the degradation of polyvinyl alcohol
physiological function
additional information
the enzyme belongs to the alpha/beta-hydrolase family and contains a unique lid region that covers the active site
evolution
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the enzyme belongs to the alpha/beta-hydrolase family and contains a unique lid region that covers the active site
evolution
the enzyme belongs to the alpha/beta-hydrolase family and contains a unique lid region that covers the active site
evolution
-
the enzyme belongs to the alpha/beta-hydrolase family and contains a unique lid region that covers the active site
-
the enzyme is involved in degradation of polyvinyl alcohol
physiological function
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the enzyme is involved in degradation of polyvinyl alcohol
physiological function
the enzyme is involved in degradation of polyvinyl alcohol
physiological function
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the enzyme is involved in degradation of polyvinyl alcohol
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roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase, the lid is the most variable region of the enzyme. The disulfide bond formation of Cys257/267 is important for the activity of pOPH
additional information
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roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase, the lid is the most variable region of the enzyme. The disulfide bond formation of Cys257/267 is important for the activity of pOPH
additional information
roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase, the lid is the most variable region of the enzyme. The disulfide bond formation of Cys257/267 is not essential for sOPH, which has a shorter lid structure
additional information
substrate binding and catalysis, enzyme modeling, overview
additional information
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substrate binding and catalysis, enzyme modeling, overview
additional information
substrate binding and catalysis, enzyme modeling, overview
additional information
-
roles of tryptophan residue and disulfide bond in the variable lid region of oxidized polyvinyl alcohol hydrolase, the lid is the most variable region of the enzyme. The disulfide bond formation of Cys257/267 is important for the activity of pOPH
-
additional information
-
substrate binding and catalysis, enzyme modeling, overview
-